ID DXS_VIBC3 Reviewed; 626 AA.
AC A5F331; C3LYQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase;
DE EC=2.2.1.7;
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase;
DE Short=DXP synthase;
DE Short=DXPS;
GN Name=dxs; OrderedLocusNames=VC0395_A0412, VC395_0905;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y.,
RA Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the
RT cholera pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC 1-deoxy-D-xylulose-5-phosphate (DXP) (By similarity).
CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC deoxy-D-xylulose 5-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
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DR EMBL; CP000627; ABQ21549.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08919.1; -; Genomic_DNA.
DR RefSeq; YP_001216367.1; NC_009457.1.
DR RefSeq; YP_002819155.1; NC_012582.1.
DR ProteinModelPortal; A5F331; -.
DR SMR; A5F331; 3-625.
DR STRING; 345073.VC0395_A0412; -.
DR EnsemblBacteria; ABQ21549; ABQ21549; VC0395_A0412.
DR EnsemblBacteria; ACP08919; ACP08919; VC395_0905.
DR GeneID; 5136254; -.
DR GeneID; 7774897; -.
DR KEGG; vco:VC0395_A0412; -.
DR KEGG; vcr:VC395_0905; -.
DR eggNOG; COG1154; -.
DR HOGENOM; HOG000012988; -.
DR KO; K01662; -.
DR OMA; GDIKPDM; -.
DR ProtClustDB; PRK05444; -.
DR UniPathway; UPA00064; UER00091.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:HAMAP.
DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_00315; DXP_synth; 1; -.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF13292; DXP_synthase_N; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52922; Transketo_C_like; 1.
DR TIGRFAMs; TIGR00204; dxs; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT CHAIN 1 626 1-deoxy-D-xylulose-5-phosphate synthase.
FT /FTId=PRO_1000071998.
FT REGION 121 123 Thiamine pyrophosphate binding (By
FT similarity).
FT REGION 153 154 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 152 152 Magnesium (By similarity).
FT METAL 181 181 Magnesium (By similarity).
FT BINDING 80 80 Thiamine pyrophosphate (By similarity).
FT BINDING 181 181 Thiamine pyrophosphate (By similarity).
FT BINDING 288 288 Thiamine pyrophosphate (By similarity).
FT BINDING 370 370 Thiamine pyrophosphate (By similarity).
SQ SEQUENCE 626 AA; 68347 MW; 5E83BF99EE8C51C9 CRC64;
MTLDISKYPT LALANTPDEL RSLPKEVLPK LCDELRTYLL NSVSQSSGHL ASGLGTVELT
VALHYVYHTP FDHLIWDVGH QAYPHKILTG RRDQMPTIRQ KDGLHPFPWR EESEYDTLSV
GHSSTSISAA LGMAICAGKE GKDRKVVSVI GDGAITAGMA FEAMNHAGDV HPDMLVVLND
NEMSISENVG ALNNHLAQVL SGSLYTSIRE GGKKVLSGIP PIKELVRRTE EHLKGMVVPG
TLFEELGFNY IGPVDGHDVL ELIKTLKNMR ELKGPQFLHV MTKKGKGYAP AEKDPIGYHG
VPKFDPSHHS LPKSSNTKPT FSKIFGDFLC DMAAQDPKLM AITPAMREGS GMVRFSKEYP
SQYFDVAIAE QHAVTLATGM AIAGYHPIVA IYSTFLQRGY DQLIHDVAIM NLPVMFAIDR
AGIVGADGQT HQGAFDLSYM RCIPNMLIMA PADENECRQM LYTGHQHQGP SAVRYPRGNG
MGVELESSFT ALEIGKGRLM RESTACEGEK VAILSFGTLL PNALQAAEKL NATVADMRFV
KPLDEALIKQ LAQTHDVLVT LEENAIAGGA GAGVIEFLMK EKQLKPVLNL GLPDQFIVQG
TQEEMHAELG LDGAGIERAI RDYLAK
//
